ER & Golgi Flashcards

1
Q

what mediates folding of proteins

A

chaperone proteins

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2
Q

what mediates disulphide bridge formation in proteins

A

protein disulphide isomerase (PDI)

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3
Q

what is oligomerisation

A

the assembly of multi-protein complexes

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4
Q

what 3 things are required for ribosome docking

A

signal peptide/signal sequence (SP), signal recognition particle (SRP), SRP receptor

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5
Q

how do proteins enter the ER lumen

A

through the translocation channel (translocon)

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6
Q

what occurs during translocation in type 1 proteins

A

signal sequence is cleaved at the n terminus by signal peptidase

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7
Q

what is the defining property of stop/start transfer sequences

A

they are hydrophobic so will be found in the ER membrane

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8
Q

how is a hydropathy plot read

A

the hydrophobic areas represent the hydrophobic domains of signal sequences

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9
Q

what is an internal signal sequence

A

internal signal sequences exist in the middle of the polypeptide chain rather than the end, so are not cleaved

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10
Q

4 features of a type 1 transmembrane protein

A

single pass
cleaved signal sequence
stop sequence in the ER membrane
C terminus in cytosol

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11
Q

key difference between type 2 & type 3 TM proteins

A

orientation, N terminus in cytosol for type 2 protein, C terminus in cytosol for type 3 protein

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12
Q

what determines the orientation of the protein

A

whether positive amino acid side chains are
in front of or behind the signal sequence. If they are in front of the Signal Sequence then N terminus in cytosol
If behind the signal sequence then C terminus in cytosol

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13
Q

what are type 4 TM proteins

A

they have 2 or more transmembrane domains (stop/start sequences)

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14
Q

what are the 2 sides of the Golgi and where do they face

A

cis side faces nucleus

trans side faces nearest plasma membrane

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15
Q

what is the sequence for forward Golgi traffic

A

er to cis Golgi network to cis cisterna to medial cisterna to trans cisterna to plasma membrane

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16
Q

what is the cisternal progression model

A

enzymes move sequentially backwards from trans to cis stacks through retrograde vesicle transport, substrates stay in the same compartments

17
Q

what happens during clatherin mediated endocytosis of LDL

A

LDL binds to receptor which migrates to clatherin pit
Clathrin coated vesicle is uncoated once inside the cell
`Vesicle binds with endosome of ph5 and receptor releases LDL
Late endosome binds with lysosome and cholesterol, amino acids and small peptides form
Cholesterol is released into cytosol for new membrane formation

18
Q

how does dynamin work

A

it polymerises around the vesicle bud neck and hydrolyses GTP to cause a conformational change, this stretches the neck until the bud pinches off

19
Q

what is the difference between COP1 and COP2

A

COP1 is the protein coat involved in retrograde enzyme transport, COP2 is the protein coat involved in movement from ER to Golgi. They drive transport in opposite directions

20
Q

what is the function of SNARES

A

they are involved in the membrane fusing process, v-snare binds to t-snare to form a tight hydrophobic complex